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1. Annual (2023) taxonomic update of RNA-directed RNA polymerase-encoding negative-sense RNA viruses (realm Riboviria: kingdom Orthornavirae: phylum Negarnaviricota)

Author

Kuhn, J, Abe, J, Adkins, S, Alkhovsky, S, Avsic-Zupanc, T, Ayllon, M, Bahl, J, Balkema-Buschmann, A, Ballinger, M, Baranwal, V, Beer, M, Bejerman, N, Bergeron, E, Biedenkopf, N, Blair, C, Blasdell, K, Blouin, A, Bradfute, S, Briese, T, Brown, P, Buchholz, U, Buchmeier, M, Bukreyev, A, Burt, F, Buttner, C, Calisher, C, Cao, M, Casas, I, Chandran, K, Charrel, R, Chaturvedi, K, Chooi, K, Crane, A, Bo, E, de la Torre, J, de Souza, W, de Swart, R, Debat, H, Dheilly, N, Di Paola, N, Di Serio, F, Dietzgen, R, Digiaro, M, Drexler, J, Duprex, W, Durrwald, R, Easton, A, Elbeaino, T, Ergunay, K, Feng, G, Firth, A, Fooks, A, Formenty, P, Freitas-Astua, J, Gago-Zachert, S, Garcia, M, Garcia-Sastre, A, Garrison, A, Gaskin, T, Gong, W, Gonzalez, J, de Bellocq, J, Griffiths, A, Groschup, M, Gunther, I, Gunther, S, Hammond, J, Hasegawa, Y, Hayashi, K, Hepojoki, J, Higgins, C, Hongo, S, Horie, M, Hughes, H, Hume, A, Hyndman, T, Ikeda, K, Jiang, D, Jonson, G, Junglen, S, Klempa, B, Klingstrom, J, Kondo, H, Koonin, E, Krupovic, M, Kubota, K, Kurath, G, Laenen, L, Lambert, A, Li, J, Liu, R, Lukashevich, I, Macdiarmid, R, Maes, P, Marklewitz, M, Marshall, S, Marzano, S, Mccauley, J, Mirazimi, A, Muhlberger, E, Nabeshima, T, Naidu, R, Natsuaki, T, Navarro, B, Navarro, J, Neriya, Y, Netesov, S, Neumann, G, Nowotny, N, Nunes, M, Ochoa-Corona, F, Okada, T, Palacios, G, Pallas, V, Papa, A, Paraskevopoulou, S, Parrish, C, Pauvolid-Correa, A, Paweska, J, Perez, D, Pfaff, F, Plemper, R, Postler, T, Rabbidge, L, Radoshitzky, S, Ramos-Gonzalez, P, Rehanek, M, Resende, R, Reyes, C, Rodrigues, T, Romanowski, V, Rubbenstroth, D, Rubino, L, Runstadler, J, Sabanadzovic, S, Sadiq, S, Salvato, M, Sasaya, T, Schwemmle, M, Sharpe, S, Shi, M, Shimomoto, Y, Sidharthan, V, Sironi, M, Smither, S, Song, J, Spann, K, Spengler, J, Stenglein, M, Takada, A, Takeyama, S, Tatara, A, Tesh, R, Thornburg, N, Tian, X, Tischler, N, Tomitaka, Y, Tomonaga, K, Tordo, N, Tu, C, Turina, M, Tzanetakis, I, Vaira, A, van den Hoogen, B, Vanmechelen, B, Vasilakis, N, Verbeek, M, von Bargen, S, Wada, J, Wahl, V, Walker, P, Waltzek, T, Whitfield, A, Wolf, Y, Xia, H, Xylogianni, E, Yanagisawa, H, Yano, K, Ye, G, Yuan, Z, Zerbini, F, Zhang, G, Zhang, S, Zhang, Y, Zhao, L, Okland, A, Kuhn J. H., Abe J., Adkins S., Alkhovsky S. V., Avsic-Zupanc T., Ayllon M. A., Bahl J., Balkema-Buschmann A., Ballinger M. J., Baranwal V. K., Beer M., Bejerman N., Bergeron E., Biedenkopf N., Blair C. D., Blasdell K. R., Blouin A. G., Bradfute S. B., Briese T., Brown P. A., Buchholz U. J., Buchmeier M. J., Bukreyev A., Burt F., Buttner C., Calisher C. H., Cao M., Casas I., Chandran K., Charrel R. N., Chaturvedi K. K., Chooi K. M., Crane A., Bo E. D., de la Torre J. C., de Souza W. M., de Swart R. L., Debat H., Dheilly N. M., Di Paola N., Di Serio F., Dietzgen R. G., Digiaro M., Drexler J. F., Duprex W. P., Durrwald R., Easton A. J., Elbeaino T., Ergunay K., Feng G., Firth A. E., Fooks A. R., Formenty P. B. H., Freitas-Astua J., Gago-Zachert S., Garcia M. L., Garcia-Sastre A., Garrison A. R., Gaskin T. R., Gong W., Gonzalez J. -P. J., de Bellocq J., Griffiths A., Groschup M. H., Gunther I., Gunther S., Hammond J., Hasegawa Y., Hayashi K., Hepojoki J., Higgins C. M., Hongo S., Horie M., Hughes H. R., Hume A. J., Hyndman T. H., Ikeda K., Jiang D., Jonson G. B., Junglen S., Klempa B., Klingstrom J., Kondo H., Koonin E. V., Krupovic M., Kubota K., Kurath G., Laenen L., Lambert A. J., Li J., Li J. -M., Liu R., Lukashevich I. S., MacDiarmid R. M., Maes P., Marklewitz M., Marshall S. H., Marzano S. -Y. L., McCauley J. W., Mirazimi A., Muhlberger E., Nabeshima T., Naidu R., Natsuaki T., Navarro B., Navarro J. A., Neriya Y., Netesov S. V., Neumann G., Nowotny N., Nunes M. R. T., Ochoa-Corona F. M., Okada T., Palacios G., Pallas V., Papa A., Paraskevopoulou S., Parrish C. R., Pauvolid-Correa A., Paweska J. T., Perez D. R., Pfaff F., Plemper R. K., Postler T. S., Rabbidge L. O., Radoshitzky S. R., Ramos-Gonzalez P. L., Rehanek M., Resende R. O., Reyes C. A., Rodrigues T. C. S., Romanowski V., Rubbenstroth D., Rubino L., Runstadler J. A., Sabanadzovic S., Sadiq S., Salvato M. S., Sasaya T., Schwemmle M., Sharpe S. R., Shi M., Shimomoto Y., Sidharthan V. K., Sironi M., Smither S., Song J. -W., Spann K. M., Spengler J. R., Stenglein M. D., Takada A., Takeyama S., Tatara A., Tesh R. B., Thornburg N. J., Tian X., Tischler N. D., Tomitaka Y., Tomonaga K., Tordo N., Tu C., Turina M., Tzanetakis I. E., Vaira A. M., van den Hoogen B., Vanmechelen B., Vasilakis N., Verbeek M., von Bargen S., Wada J., Wahl V., Walker P. J., Waltzek T. B., Whitfield A. E., Wolf Y. I., Xia H., Xylogianni E., Yanagisawa H., Yano K., Ye G., Yuan Z., Zerbini F. M., Zhang G., Zhang S., Zhang Y. -Z., Zhao L., Okland A. L., Kuhn, J, Abe, J, Adkins, S, Alkhovsky, S, Avsic-Zupanc, T, Ayllon, M, Bahl, J, Balkema-Buschmann, A, Ballinger, M, Baranwal, V, Beer, M, Bejerman, N, Bergeron, E, Biedenkopf, N, Blair, C, Blasdell, K, Blouin, A, Bradfute, S, Briese, T, Brown, P, Buchholz, U, Buchmeier, M, Bukreyev, A, Burt, F, Buttner, C, Calisher, C, Cao, M, Casas, I, Chandran, K, Charrel, R, Chaturvedi, K, Chooi, K, Crane, A, Bo, E, de la Torre, J, de Souza, W, de Swart, R, Debat, H, Dheilly, N, Di Paola, N, Di Serio, F, Dietzgen, R, Digiaro, M, Drexler, J, Duprex, W, Durrwald, R, Easton, A, Elbeaino, T, Ergunay, K, Feng, G, Firth, A, Fooks, A, Formenty, P, Freitas-Astua, J, Gago-Zachert, S, Garcia, M, Garcia-Sastre, A, Garrison, A, Gaskin, T, Gong, W, Gonzalez, J, de Bellocq, J, Griffiths, A, Groschup, M, Gunther, I, Gunther, S, Hammond, J, Hasegawa, Y, Hayashi, K, Hepojoki, J, Higgins, C, Hongo, S, Horie, M, Hughes, H, Hume, A, Hyndman, T, Ikeda, K, Jiang, D, Jonson, G, Junglen, S, Klempa, B, Klingstrom, J, Kondo, H, Koonin, E, Krupovic, M, Kubota, K, Kurath, G, Laenen, L, Lambert, A, Li, J, Liu, R, Lukashevich, I, Macdiarmid, R, Maes, P, Marklewitz, M, Marshall, S, Marzano, S, Mccauley, J, Mirazimi, A, Muhlberger, E, Nabeshima, T, Naidu, R, Natsuaki, T, Navarro, B, Navarro, J, Neriya, Y, Netesov, S, Neumann, G, Nowotny, N, Nunes, M, Ochoa-Corona, F, Okada, T, Palacios, G, Pallas, V, Papa, A, Paraskevopoulou, S, Parrish, C, Pauvolid-Correa, A, Paweska, J, Perez, D, Pfaff, F, Plemper, R, Postler, T, Rabbidge, L, Radoshitzky, S, Ramos-Gonzalez, P, Rehanek, M, Resende, R, Reyes, C, Rodrigues, T, Romanowski, V, Rubbenstroth, D, Rubino, L, Runstadler, J, Sabanadzovic, S, Sadiq, S, Salvato, M, Sasaya, T, Schwemmle, M, Sharpe, S, Shi, M, Shimomoto, Y, Sidharthan, V, Sironi, M, Smither, S, Song, J, Spann, K, Spengler, J, Stenglein, M, Takada, A, Takeyama, S, Tatara, A, Tesh, R, Thornburg, N, Tian, X, Tischler, N, Tomitaka, Y, Tomonaga, K, Tordo, N, Tu, C, Turina, M, Tzanetakis, I, Vaira, A, van den Hoogen, B, Vanmechelen, B, Vasilakis, N, Verbeek, M, von Bargen, S, Wada, J, Wahl, V, Walker, P, Waltzek, T, Whitfield, A, Wolf, Y, Xia, H, Xylogianni, E, Yanagisawa, H, Yano, K, Ye, G, Yuan, Z, Zerbini, F, Zhang, G, Zhang, S, Zhang, Y, Zhao, L, Okland, A, Kuhn J. H., Abe J., Adkins S., Alkhovsky S. V., Avsic-Zupanc T., Ayllon M. A., Bahl J., Balkema-Buschmann A., Ballinger M. J., Baranwal V. K., Beer M., Bejerman N., Bergeron E., Biedenkopf N., Blair C. D., Blasdell K. R., Blouin A. G., Bradfute S. B., Briese T., Brown P. A., Buchholz U. J., Buchmeier M. J., Bukreyev A., Burt F., Buttner C., Calisher C. H., Cao M., Casas I., Chandran K., Charrel R. N., Chaturvedi K. K., Chooi K. M., Crane A., Bo E. D., de la Torre J. C., de Souza W. M., de Swart R. L., Debat H., Dheilly N. M., Di Paola N., Di Serio F., Dietzgen R. G., Digiaro M., Drexler J. F., Duprex W. P., Durrwald R., Easton A. J., Elbeaino T., Ergunay K., Feng G., Firth A. E., Fooks A. R., Formenty P. B. H., Freitas-Astua J., Gago-Zachert S., Garcia M. L., Garcia-Sastre A., Garrison A. R., Gaskin T. R., Gong W., Gonzalez J. -P. J., de Bellocq J., Griffiths A., Groschup M. H., Gunther I., Gunther S., Hammond J., Hasegawa Y., Hayashi K., Hepojoki J., Higgins C. M., Hongo S., Horie M., Hughes H. R., Hume A. J., Hyndman T. H., Ikeda K., Jiang D., Jonson G. B., Junglen S., Klempa B., Klingstrom J., Kondo H., Koonin E. V., Krupovic M., Kubota K., Kurath G., Laenen L., Lambert A. J., Li J., Li J. -M., Liu R., Lukashevich I. S., MacDiarmid R. M., Maes P., Marklewitz M., Marshall S. H., Marzano S. -Y. L., McCauley J. W., Mirazimi A., Muhlberger E., Nabeshima T., Naidu R., Natsuaki T., Navarro B., Navarro J. A., Neriya Y., Netesov S. V., Neumann G., Nowotny N., Nunes M. R. T., Ochoa-Corona F. M., Okada T., Palacios G., Pallas V., Papa A., Paraskevopoulou S., Parrish C. R., Pauvolid-Correa A., Paweska J. T., Perez D. R., Pfaff F., Plemper R. K., Postler T. S., Rabbidge L. O., Radoshitzky S. R., Ramos-Gonzalez P. L., Rehanek M., Resende R. O., Reyes C. A., Rodrigues T. C. S., Romanowski V., Rubbenstroth D., Rubino L., Runstadler J. A., Sabanadzovic S., Sadiq S., Salvato M. S., Sasaya T., Schwemmle M., Sharpe S. R., Shi M., Shimomoto Y., Sidharthan V. K., Sironi M., Smither S., Song J. -W., Spann K. M., Spengler J. R., Stenglein M. D., Takada A., Takeyama S., Tatara A., Tesh R. B., Thornburg N. J., Tian X., Tischler N. D., Tomitaka Y., Tomonaga K., Tordo N., Tu C., Turina M., Tzanetakis I. E., Vaira A. M., van den Hoogen B., Vanmechelen B., Vasilakis N., Verbeek M., von Bargen S., Wada J., Wahl V., Walker P. J., Waltzek T. B., Whitfield A. E., Wolf Y. I., Xia H., Xylogianni E., Yanagisawa H., Yano K., Ye G., Yuan Z., Zerbini F. M., Zhang G., Zhang S., Zhang Y. -Z., Zhao L., and Okland A. L.

Abstract

In April 2023, following the annual International Committee on Taxonomy of Viruses (ICTV) ratification vote on newly proposed taxa, the phylum Negarnaviricota was amended and emended. The phylum was expanded by one new family, 14 new genera, and 140 new species. Two genera and 538 species were renamed. One species was moved, and four were abolished. This article presents the updated taxonomy of Negarnaviricota as now accepted by the ICTV

Published
2023

3. 2022 taxonomic update of phylum Negarnaviricota (Riboviria: Orthornavirae), including the large orders Bunyavirales and Mononegavirales

Author

Kuhn, J, Adkins, S, Alkhovsky, S, Avšič-Županc, T, Ayllón, M, Bahl, J, Balkema-Buschmann, A, Ballinger, M, Bandte, M, Beer, M, Bejerman, N, Bergeron, É, Biedenkopf, N, Bigarré, L, Blair, C, Blasdell, K, Bradfute, S, Briese, T, Brown, P, Bruggmann, R, Buchholz, U, Buchmeier, M, Bukreyev, A, Burt, F, Büttner, C, Calisher, C, Candresse, T, Carson, J, Casas, I, Chandran, K, Charrel, R, Chiaki, Y, Crane, A, Crane, M, Dacheux, L, Bó, E, de la Torre, J, de Lamballerie, X, de Souza, W, de Swart, R, Dheilly, N, Di Paola, N, Di Serio, F, Dietzgen, R, Digiaro, M, Drexler, J, Duprex, W, Dürrwald, R, Easton, A, Elbeaino, T, Ergünay, K, Feng, G, Feuvrier, C, Firth, A, Fooks, A, Formenty, P, Freitas-Astúa, J, Gago-Zachert, S, García, M, García-Sastre, A, Garrison, A, Godwin, S, Gonzalez, J, de Bellocq, J, Griffiths, A, Groschup, M, Günther, S, Hammond, J, Hepojoki, J, Hierweger, M, Hongō, S, Horie, M, Horikawa, H, Hughes, H, Hume, A, Hyndman, T, Jiāng, D, Jonson, G, Junglen, S, Kadono, F, Karlin, D, Klempa, B, Klingström, J, Koch, M, Kondō, H, Koonin, E, Krásová, J, Krupovic, M, Kubota, K, Kuzmin, I, Laenen, L, Lambert, A, Lǐ, J, Li, J, Lieffrig, F, Lukashevich, I, Luo, D, Maes, P, Marklewitz, M, Marshall, S, Marzano, S, Mccauley, J, Mirazimi, A, Mohr, P, Moody, N, Morita, Y, Morrison, R, Mühlberger, E, Naidu, R, Natsuaki, T, Navarro, J, Neriya, Y, Netesov, S, Neumann, G, Nowotny, N, Ochoa-Corona, F, Palacios, G, Pallandre, L, Pallás, V, Papa, A, Paraskevopoulou, S, Parrish, C, Pauvolid-Corrêa, A, Pawęska, J, Pérez, D, Pfaff, F, Plemper, R, Postler, T, Pozet, F, Radoshitzky, S, Ramos-González, P, Rehanek, M, Resende, R, Reyes, C, Romanowski, V, Rubbenstroth, D, Rubino, L, Rumbou, A, Runstadler, J, Rupp, M, Sabanadzovic, S, Sasaya, T, Schmidt-Posthaus, H, Schwemmle, M, Seuberlich, T, Sharpe, S, Shi, M, Sironi, M, Smither, S, Song, J, Spann, K, Spengler, J, Stenglein, M, Takada, A, Tesh, R, Těšíková, J, Thornburg, N, Tischler, N, Tomitaka, Y, Tomonaga, K, Tordo, N, Tsunekawa, K, Turina, M, Tzanetakis, I, Vaira, A, van den Hoogen, B, Vanmechelen, B, Vasilakis, N, Verbeek, M, von Bargen, S, Wada, J, Wahl, V, Walker, P, Whitfield, A, Williams, J, Wolf, Y, Yamasaki, J, Yanagisawa, H, Ye, G, Zhang, Y, Økland, A, Kuhn JH, Adkins S, Alkhovsky SV, Avšič-Županc T, Ayllón MA, Bahl J, Balkema-Buschmann A, Ballinger MJ, Bandte M, Beer M, Bejerman N, Bergeron É, Biedenkopf N, Bigarré L, Blair CD, Blasdell KR, Bradfute SB, Briese T, Brown PA, Bruggmann R, Buchholz UJ, Buchmeier MJ, Bukreyev A, Burt F, Büttner C, Calisher CH, Candresse T, Carson J, Casas I, Chandran K, Charrel RN, Chiaki Y, Crane A, Crane M, Dacheux L, Bó ED, de la Torre JC, de Lamballerie X, de Souza WM, de Swart RL, Dheilly NM, Di Paola N, Di Serio F, Dietzgen RG, Digiaro M, Drexler JF, Duprex WP, Dürrwald R, Easton AJ, Elbeaino T, Ergünay K, Feng G, Feuvrier C, Firth AE, Fooks AR, Formenty PBH, Freitas-Astúa J, Gago-Zachert S, García ML, García-Sastre A, Garrison AR, Godwin SE, Gonzalez JJ, de Bellocq JG, Griffiths A, Groschup MH, Günther S, Hammond J, Hepojoki J, Hierweger MM, Hongō S, Horie M, Horikawa H, Hughes HR, Hume AJ, Hyndman TH, Jiāng D, Jonson GB, Junglen S, Kadono F, Karlin DG, Klempa B, Klingström J, Koch MC, Kondō H, Koonin EV, Krásová J, Krupovic M, Kubota K, Kuzmin IV, Laenen L, Lambert AJ, Lǐ J, Li JM, Lieffrig F, Lukashevich IS, Luo D, Maes P, Marklewitz M, Marshall SH, Marzano SL, McCauley JW, Mirazimi A, Mohr PG, Moody NJG, Morita Y, Morrison RN, Mühlberger E, Naidu R, Natsuaki T, Navarro JA, Neriya Y, Netesov SV, Neumann G, Nowotny N, Ochoa-Corona FM, Palacios G, Pallandre L, Pallás V, Papa A, Paraskevopoulou S, Parrish CR, Pauvolid-Corrêa A, Pawęska JT, Pérez DR, Pfaff F, Plemper RK, Postler TS, Pozet F, Radoshitzky SR, Ramos-González PL, Rehanek M, Resende RO, Reyes CA, Romanowski V, Rubbenstroth D, Rubino L, Rumbou A, Runstadler JA, Rupp M, Sabanadzovic S, Sasaya T, Schmidt-Posthaus H, Schwemmle M, Seuberlich T, Sharpe SR, Shi M, Sironi M, Smither S, Song JW, Spann KM, Spengler JR, Stenglein MD, Takada A, Tesh RB, Těšíková J, Thornburg NJ, Tischler ND, Tomitaka Y, Tomonaga K, Tordo N, Tsunekawa K, Turina M, Tzanetakis IE, Vaira AM, van den Hoogen B, Vanmechelen B, Vasilakis N, Verbeek M, von Bargen S, Wada J, Wahl V, Walker PJ, Whitfield AE, Williams JV, Wolf YI, Yamasaki J, Yanagisawa H, Ye G, Zhang YZ, Økland AL., Kuhn, J, Adkins, S, Alkhovsky, S, Avšič-Županc, T, Ayllón, M, Bahl, J, Balkema-Buschmann, A, Ballinger, M, Bandte, M, Beer, M, Bejerman, N, Bergeron, É, Biedenkopf, N, Bigarré, L, Blair, C, Blasdell, K, Bradfute, S, Briese, T, Brown, P, Bruggmann, R, Buchholz, U, Buchmeier, M, Bukreyev, A, Burt, F, Büttner, C, Calisher, C, Candresse, T, Carson, J, Casas, I, Chandran, K, Charrel, R, Chiaki, Y, Crane, A, Crane, M, Dacheux, L, Bó, E, de la Torre, J, de Lamballerie, X, de Souza, W, de Swart, R, Dheilly, N, Di Paola, N, Di Serio, F, Dietzgen, R, Digiaro, M, Drexler, J, Duprex, W, Dürrwald, R, Easton, A, Elbeaino, T, Ergünay, K, Feng, G, Feuvrier, C, Firth, A, Fooks, A, Formenty, P, Freitas-Astúa, J, Gago-Zachert, S, García, M, García-Sastre, A, Garrison, A, Godwin, S, Gonzalez, J, de Bellocq, J, Griffiths, A, Groschup, M, Günther, S, Hammond, J, Hepojoki, J, Hierweger, M, Hongō, S, Horie, M, Horikawa, H, Hughes, H, Hume, A, Hyndman, T, Jiāng, D, Jonson, G, Junglen, S, Kadono, F, Karlin, D, Klempa, B, Klingström, J, Koch, M, Kondō, H, Koonin, E, Krásová, J, Krupovic, M, Kubota, K, Kuzmin, I, Laenen, L, Lambert, A, Lǐ, J, Li, J, Lieffrig, F, Lukashevich, I, Luo, D, Maes, P, Marklewitz, M, Marshall, S, Marzano, S, Mccauley, J, Mirazimi, A, Mohr, P, Moody, N, Morita, Y, Morrison, R, Mühlberger, E, Naidu, R, Natsuaki, T, Navarro, J, Neriya, Y, Netesov, S, Neumann, G, Nowotny, N, Ochoa-Corona, F, Palacios, G, Pallandre, L, Pallás, V, Papa, A, Paraskevopoulou, S, Parrish, C, Pauvolid-Corrêa, A, Pawęska, J, Pérez, D, Pfaff, F, Plemper, R, Postler, T, Pozet, F, Radoshitzky, S, Ramos-González, P, Rehanek, M, Resende, R, Reyes, C, Romanowski, V, Rubbenstroth, D, Rubino, L, Rumbou, A, Runstadler, J, Rupp, M, Sabanadzovic, S, Sasaya, T, Schmidt-Posthaus, H, Schwemmle, M, Seuberlich, T, Sharpe, S, Shi, M, Sironi, M, Smither, S, Song, J, Spann, K, Spengler, J, Stenglein, M, Takada, A, Tesh, R, Těšíková, J, Thornburg, N, Tischler, N, Tomitaka, Y, Tomonaga, K, Tordo, N, Tsunekawa, K, Turina, M, Tzanetakis, I, Vaira, A, van den Hoogen, B, Vanmechelen, B, Vasilakis, N, Verbeek, M, von Bargen, S, Wada, J, Wahl, V, Walker, P, Whitfield, A, Williams, J, Wolf, Y, Yamasaki, J, Yanagisawa, H, Ye, G, Zhang, Y, Økland, A, Kuhn JH, Adkins S, Alkhovsky SV, Avšič-Županc T, Ayllón MA, Bahl J, Balkema-Buschmann A, Ballinger MJ, Bandte M, Beer M, Bejerman N, Bergeron É, Biedenkopf N, Bigarré L, Blair CD, Blasdell KR, Bradfute SB, Briese T, Brown PA, Bruggmann R, Buchholz UJ, Buchmeier MJ, Bukreyev A, Burt F, Büttner C, Calisher CH, Candresse T, Carson J, Casas I, Chandran K, Charrel RN, Chiaki Y, Crane A, Crane M, Dacheux L, Bó ED, de la Torre JC, de Lamballerie X, de Souza WM, de Swart RL, Dheilly NM, Di Paola N, Di Serio F, Dietzgen RG, Digiaro M, Drexler JF, Duprex WP, Dürrwald R, Easton AJ, Elbeaino T, Ergünay K, Feng G, Feuvrier C, Firth AE, Fooks AR, Formenty PBH, Freitas-Astúa J, Gago-Zachert S, García ML, García-Sastre A, Garrison AR, Godwin SE, Gonzalez JJ, de Bellocq JG, Griffiths A, Groschup MH, Günther S, Hammond J, Hepojoki J, Hierweger MM, Hongō S, Horie M, Horikawa H, Hughes HR, Hume AJ, Hyndman TH, Jiāng D, Jonson GB, Junglen S, Kadono F, Karlin DG, Klempa B, Klingström J, Koch MC, Kondō H, Koonin EV, Krásová J, Krupovic M, Kubota K, Kuzmin IV, Laenen L, Lambert AJ, Lǐ J, Li JM, Lieffrig F, Lukashevich IS, Luo D, Maes P, Marklewitz M, Marshall SH, Marzano SL, McCauley JW, Mirazimi A, Mohr PG, Moody NJG, Morita Y, Morrison RN, Mühlberger E, Naidu R, Natsuaki T, Navarro JA, Neriya Y, Netesov SV, Neumann G, Nowotny N, Ochoa-Corona FM, Palacios G, Pallandre L, Pallás V, Papa A, Paraskevopoulou S, Parrish CR, Pauvolid-Corrêa A, Pawęska JT, Pérez DR, Pfaff F, Plemper RK, Postler TS, Pozet F, Radoshitzky SR, Ramos-González PL, Rehanek M, Resende RO, Reyes CA, Romanowski V, Rubbenstroth D, Rubino L, Rumbou A, Runstadler JA, Rupp M, Sabanadzovic S, Sasaya T, Schmidt-Posthaus H, Schwemmle M, Seuberlich T, Sharpe SR, Shi M, Sironi M, Smither S, Song JW, Spann KM, Spengler JR, Stenglein MD, Takada A, Tesh RB, Těšíková J, Thornburg NJ, Tischler ND, Tomitaka Y, Tomonaga K, Tordo N, Tsunekawa K, Turina M, Tzanetakis IE, Vaira AM, van den Hoogen B, Vanmechelen B, Vasilakis N, Verbeek M, von Bargen S, Wada J, Wahl V, Walker PJ, Whitfield AE, Williams JV, Wolf YI, Yamasaki J, Yanagisawa H, Ye G, Zhang YZ, and Økland AL.

Abstract

In March 2022, following the annual International Committee on Taxonomy of Viruses (ICTV) ratification vote on newly proposed taxa, the phylum Negarnaviricota was amended and emended. The phylum was expanded by two new families (bunyaviral Discoviridae and Tulasviridae), 41 new genera, and 98 new species. Three hundred forty-nine species were renamed and/or moved. The accidentally misspelled names of seven species were corrected. This article presents the updated taxonomy of Negarnaviricota as now accepted by the ICTV.

Published
2022

7. Capturing Enveloped Viruses on Affinity Grids for Downstream Cryo- Electron Microscopy Applications

Author

Kiss, G., Chen, X. M., Brindley, M. A., Campbell, P., Afonso, C. L., Ke, Z. L., Holl, J. M., Guerrero-Ferreira, R. C., Byrd-Leotis, L. A., Steel, J., Steinhauer, D. A., Plemper, R. K., Kelly, Deborah F., Spearman, P. W., Wright, E. R., Kiss, G., Chen, X. M., Brindley, M. A., Campbell, P., Afonso, C. L., Ke, Z. L., Holl, J. M., Guerrero-Ferreira, R. C., Byrd-Leotis, L. A., Steel, J., Steinhauer, D. A., Plemper, R. K., Kelly, Deborah F., Spearman, P. W., and Wright, E. R.

Abstract

Electron microscopy (EM), cryo-electron microscopy (cryo-EM), and cryo-electron tomography (cryo-ET) are essential techniques used for characterizing basic virus morphology and determining the three-dimensional structure of viruses. Enveloped viruses, which contain an outer lipoprotein coat, constitute the largest group of pathogenic viruses to humans. The purification of enveloped viruses from cell culture presents certain challenges. Specifically, the inclusion of host-membrane-derived vesicles, the complete destruction of the viruses, and the disruption of the internal architecture of individual virus particles. Here, we present a strategy for capturing enveloped viruses on affinity grids (AG) for use in both conventional EM and cryo-EM/ET applications. We examined the utility of AG for the selective capture of human immunodeficiency virus virus-like particles, influenza A, and measles virus. We applied nickel-nitrilotriacetic acid lipid layers in combination with molecular adaptors to selectively adhere the viruses to the AG surface. This further development of the AG method may prove essential for the gentle and selective purification of enveloped viruses directly onto EM grids for ultrastructural analyses.

Published
2014
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9. A CD46CD[55–46] chimeric receptor, eight short consensus repeats long, acts as an inhibitor of both CD46 (MCP)- and CD150 (SLAM)-mediated cell–cell fusion induced by CD46-using measles virus

Author

Plemper, R., Hammond, A., Fielding, A., Cattaneo, R., Lanteri, Marc, Gerlier, D., De Sousa, Emmanuel, Christiansen, Dale, Kyriakou, Peter, Loveland, Bruce, Wild, Fabian, AstraZeneca, Virologie et pathogenèse virale (VPV), Centre National de la Recherche Scientifique (CNRS)-Université Claude Bernard Lyon 1 (UCBL), Université de Lyon-Université de Lyon, Immunite et Vaccination, and Institut National de la Santé et de la Recherche Médicale (INSERM)

Subjects
Repetitive Sequences, Amino Acid, viruses, Recombinant Fusion Proteins, Molecular Sequence Data, Immunoglobulins, Receptors, Cell Surface, CHO Cells, Biology, Membrane Fusion, Cell membrane, Measles virus, Membrane Cofactor Protein, Signaling Lymphocytic Activation Molecule Family Member 1, Antigens, CD, Virology, Cricetinae, medicine, Animals, Amino Acid Sequence, Binding site, Receptor, ComputingMilieux_MISCELLANEOUS, Glycoproteins, Membrane Glycoproteins, CD46, biology.organism_classification, female genital diseases and pregnancy complications, Transmembrane protein, medicine.anatomical_structure, Viral replication, Cytoplasm, [SDV.MP.VIR]Life Sciences [q-bio]/Microbiology and Parasitology/Virology
Abstract

According to their cellular receptor use, measles virus (MV) strains can be separated into two phenotypes, CD46-using and CD46-non-using. A long chimeric receptor, CD46CD[55–46], was generated from the CD46 backbone, encompassing the four short consensus repeat (SCR) domains of CD46 linked via a flexible glycine hinge to SCR1 and SCR2 of CD55, SCR3 and SCR4 of CD46 and the STP, transmembrane and cytoplasmic tail of CD46. This chimeric receptor was proficient for MV binding but deficient in mediating MV-induced cell-to-cell fusion and virus replication, possibly due to the extended distance between the MV haemagglutinin (H) binding site (CD46 SCR1–SCR2) and the cell membrane. When coexpressed with either wild-type CD46 or CD150, this fusion-incompetent receptor exerted a dominant negative effect and inhibited both cell-to-cell fusion and entry of MV with CD46-using, but not CD46-non-using, phenotype. A soluble octameric CD46–C4bpα exhibited similar CD46- and CD150-mediated fusion inhibition properties only against CD46-using MV. This suggests that the long CD46CD[55–46] receptor acts by sequestering incoming MV prior to its binding to the shorter functional CD46 or CD150 receptor.

Published
2002
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11. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.

Author

J, Bordallo, K, Plemper R, A, Finger, and H, Wolf D

Abstract

We have studied components of the endoplasmic reticulum (ER) proofreading and degradation system in the yeast Saccharomyces cerevisiae. Using a der3-1 mutant defective in the degradation of a mutated lumenal protein, carboxypeptidase yscY (CPY*), a gene was cloned which encodes a 64-kDa protein of the ER membrane. Der3p was found to be identical with Hrd1p, a protein identified to be necessary for degradation of HMG-CoA reductase. Der3p contains five putative transmembrane domains and a long hydrophilic C-terminal tail containing a RING-H2 finger domain which is oriented to the ER lumen. Deletion of DER3 leads to an accumulation of CPY* inside the ER due to a complete block of its degradation. In addition, a DER3 null mutant allele suppresses the temperature-dependent growth phenotype of a mutant carrying the sec61-2 allele. This is accompanied by the stabilization of the Sec61-2 mutant protein. In contrast, overproduction of Der3p is lethal in a sec61-2 strain at the permissive temperature of 25 degrees C. A mutant Der3p lacking 114 amino acids of the lumenal tail including the RING-H2 finger domain is unable to mediate degradation of CPY* and Sec61-2p. We propose that Der3p acts prior to retrograde transport of ER membrane and lumenal proteins to the cytoplasm where they are subject to degradation via the ubiquitin-proteasome system. Interestingly, in ubc6-ubc7 double mutants, CPY* accumulates in the ER, indicating the necessity of an intact cytoplasmic proteolysis machinery for retrograde transport of CPY*. Der3p might serve as a component programming the translocon for retrograde transport of ER proteins, or it might be involved in recognition through its lumenal RING-H2 motif of proteins of the ER that are destined for degradation.

Published
1998

12. Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome.

Author

Plemper, R K, Egner, R, Kuchler, K, and Wolf, D H

Abstract

Degradation of misfolded or tightly regulated proteins in the endoplasmic reticulum (ER) is performed by the cytosolic ubiquitin-proteasome system and therefore requires their prior transport back to the cytosol. Here, we report on the extraction and degradation mechanism of a polytopic membrane protein. Rapid proteasomal degradation of a mutated form of the ATP-binding cassette transporter Pdr5 retained in the ER is initialized at the lumenal face of the ER membrane. Using different antibodies directed against the cytosolic tails or a lumenal loop of the transmembrane protein, it could be demonstrated that the turnover of Pdr5* demands the concerted action of both the Sec61 translocon and the ubiquitin-proteasome system. We observed a stabilization of the entire molecule within the ER membrane in yeast mutants characterized by a reduced translocation capacity or by functionally attenuated proteasomes. Moreover, no degradation intermediates were detected in any of the mutants that impede degradation of Pdr5*. Therefore, initial steps are rate-limiting for cleavage and mutations that impede downstream events prevent initiation of the process. Our data suggest that ER degradation is a mechanistically highly integrated process, requiring the combined operation of components of the degradation system acting at the lumenal face of the ER membrane, the Sec61 translocon, and the ubiquitin-proteasome system.

Published
1998

13. Virology under the Microscope-a Call for Rational Discourse.

Author

Goodrum F, Lowen AC, Lakdawala S, Alwine J, Casadevall A, Imperiale MJ, Atwood W, Avgousti D, Baines J, Banfield B, Banks L, Bhaduri-McIntosh S, Bhattacharya D, Blanco-Melo D, Bloom D, Boon A, Boulant S, Brandt C, Broadbent A, Brooke C, Cameron C, Campos S, Caposio P, Chan G, Cliffe A, Coffin J, Collins K, Damania B, Daugherty M, Debbink K, DeCaprio J, Dermody T, Dikeakos J, DiMaio D, Dinglasan R, Duprex WP, Dutch R, Elde N, Emerman M, Enquist L, Fane B, Fernandez-Sesma A, Flenniken M, Frappier L, Frieman M, Frueh K, Gack M, Gaglia M, Gallagher T, Galloway D, García-Sastre A, Geballe A, Glaunsinger B, Goff S, Greninger A, Hancock M, Harris E, Heaton N, Heise M, Heldwein E, Hogue B, Horner S, Hutchinson E, Hyser J, Jackson W, Kalejta R, Kamil J, Karst S, Kirchhoff F, Knipe D, Kowalik T, Lagunoff M, Laimins L, Langlois R, Lauring A, Lee B, Leib D, Liu SL, Longnecker R, Lopez C, Luftig M, Lund J, Manicassamy B, McFadden G, McIntosh M, Mehle A, Miller WA, Mohr I, Moody C, Moorman N, Moscona A, Mounce B, Munger J, Münger K, Murphy E, Naghavi M, Nelson J, Neufeldt C, Nikolich J, O'Connor C, Ono A, Orenstein W, Ornelles D, Ou JH, Parker J, Parrish C, Pekosz A, Pellett P, Pfeiffer J, Plemper R, Polyak S, Purdy J, Pyeon D, Quinones-Mateu M, Renne R, Rice C, Schoggins J, Roller R, Russell C, Sandri-Goldin R, Sapp M, Schang L, Schmid S, Schultz-Cherry S, Semler B, Shenk T, Silvestri G, Simon V, Smith G, Smith J, Spindler K, Stanifer M, Subbarao K, Sundquist W, Suthar M, Sutton T, Tai A, Tarakanova V, tenOever B, Tibbetts S, Tompkins S, Toth Z, van Doorslaer K, Vignuzzi M, Wallace N, Walsh D, Weekes M, Weinberg J, Weitzman M, Weller S, Whelan S, White E, Williams B, Wobus C, Wong S, and Yurochko A

Subjects
Humans, SARS-CoV-2, Pandemics prevention & control, Antiviral Agents, COVID-19 prevention & control, Viruses
Abstract

Viruses have brought humanity many challenges: respiratory infection, cancer, neurological impairment and immunosuppression to name a few. Virology research over the last 60+ years has responded to reduce this disease burden with vaccines and antivirals. Despite this long history, the COVID-19 pandemic has brought unprecedented attention to the field of virology. Some of this attention is focused on concern about the safe conduct of research with human pathogens. A small but vocal group of individuals has seized upon these concerns - conflating legitimate questions about safely conducting virus-related research with uncertainties over the origins of SARS-CoV-2. The result has fueled public confusion and, in many instances, ill-informed condemnation of virology. With this article, we seek to promote a return to rational discourse. We explain the use of gain-of-function approaches in science, discuss the possible origins of SARS-CoV-2 and outline current regulatory structures that provide oversight for virological research in the United States. By offering our expertise, we - a broad group of working virologists - seek to aid policy makers in navigating these controversial issues. Balanced, evidence-based discourse is essential to addressing public concern while maintaining and expanding much-needed research in virology.

Published
2023
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14. Zoonotic potential of a novel bat morbillivirus.

Author

Lee B, Ikegame S, Carmichael J, Wells H, Furler R, Acklin J, Chiu HP, Oguntuyo K, Cox R, Patel A, Kowdle S, Stevens C, Eckley M, Zhan S, Lim J, Hashiguchi T, Durigon EL, Schountz T, Epstein J, Plemper R, Daszak P, and Anthony S

Abstract

Bats are significant reservoir hosts for many viruses with zoonotic potential1. SARS-CoV-2, Ebola virus, and Nipah virus are examples of such viruses that have caused deadly epidemics and pandemics when spilled over from bats into human and animal populations2,3. Careful surveillance of viruses in bats is critical for identifying potential zoonotic pathogens. However, metagenomic surveys in bats often do not result in full-length viral sequences that can be used to regenerate such viruses for targeted characterization4. Here, we identify and characterize a novel morbillivirus from a vespertilionid bat species (Myotis riparius) in Brazil, which we term myotis bat morbillivirus (MBaMV). There are 7 species of morbilliviruses including measles virus (MeV), canine distemper virus (CDV) and rinderpest virus (RPV)5. All morbilliviruses cause severe disease in their natural hosts6-10, and pathogenicity is largely determined by species specific expression of canonical morbillivirus receptors, CD150/SLAMF111 and NECTIN412. MBaMV used Myotis spp CD150 much better than human and dog CD150 in fusion assays. We confirmed this using live MBaMV that was rescued by reverse genetics. Surprisingly, MBaMV replicated efficiently in primary human myeloid but not lymphoid cells. Furthermore, MBaMV replicated in human epithelial cells and used human NECTIN4 almost as well as MeV. Our results demonstrate the unusual ability of MBaMV to infect and replicate in some human cells that are critical for MeV pathogenesis and transmission. This raises the specter of zoonotic transmission of a bat morbillivirus.

Published
2021
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15. Measles virus envelope glycoproteins hetero-oligomerize in the endoplasmic reticulum.

Author

Plemper RK, Hammond AL, and Cattaneo R

Subjects
Animals, Base Sequence, Biopolymers, Chlorocebus aethiops, DNA Primers, Kinetics, Mutation, Precipitin Tests, Vero Cells, Endoplasmic Reticulum metabolism, Glycoproteins metabolism, Measles virus metabolism, Viral Envelope Proteins metabolism
Abstract

The endoplasmic reticulum (ER) was investigated as the initial oligomerization site for the envelope glycoproteins H and F of measles virus (MV), a clinically relevant member of the Paramyxoviridae family, and consequences of this interaction for viral replication were studied. Both proteins were tagged at their cytosolic tails with RRR and KKXX motifs, respectively, resulting in their efficient retention in the ER. Co-transfection of the retained constructs with transport competent MV glycoproteins revealed a dominant negative effect on their biological activity indicating intracellular complex formation and thus retention. Pulse-chase analysis and co-immunoprecipitation experiments demonstrated that this effect is based on both homo- and hetero-oligomerization in the ER. Recombinant viruses additionally expressing ER-retained F showed an altered cytopathic phenotype accompanied by greatly reduced particle release. Similar mutant viruses additionally expressing ER-retained H could not be rescued indicating an even greater negative effect of this protein on virus viability. Our study suggests that both homo- and hetero-oligomerization of MV glycoproteins occur in the ER and that these events are of significance for early steps of particle assembly.

Published
2001
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16. Single-chain antibody displayed on a recombinant measles virus confers entry through the tumor-associated carcinoembryonic antigen.

Author

Hammond AL, Plemper RK, Zhang J, Schneider U, Russell SJ, and Cattaneo R

Subjects
Animals, Antibodies genetics, Antibodies immunology, Antigens, CD analysis, Cell Line, Flow Cytometry, Giant Cells physiology, Hemagglutinins, Viral genetics, Hemagglutinins, Viral immunology, Humans, Measles virus immunology, Measles virus physiology, Membrane Cofactor Protein, Membrane Glycoproteins analysis, Recombinant Fusion Proteins metabolism, Transfection, Antibodies metabolism, Carcinoembryonic Antigen immunology, Carcinoembryonic Antigen metabolism, Hemagglutinins, Viral metabolism, Measles virus genetics, Recombination, Genetic
Abstract

To redirect the tropism of the vaccine strain of measles virus (MV), Edmonston B, to a targeted cell population, we displayed on the viral hemagglutinin (H) a single-chain antibody (scAb) specific for the tumor-associated carcinoembryonic antigen (CEA). We generated H fusion proteins with three forms of the scAb appended, differing in the lengths of the linkers separating the VH and VL domains and thus in the oligomerization states of the scAbs. All proteins were stable, appeared properly folded, and were transported to the cell surface, but only H displaying the long-linker form of scAb was functional in supporting cell-cell fusion. This protein induced extensive syncytia in cells expressing the normal virus receptor CD46 and also in CD46-negative cells expressing the targeted receptor, human CEA. Replication-competent MV with H replaced by H displaying the long-linker form of scAb was recovered and replicated efficiently in both CD46-positive and CD46-negative, CEA-positive cells. Thus, MV not only tolerates the addition of a scAb on its H protein but also infects cells via a novel interaction between the scAb and its targeted receptor.

Published
2001
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17. Characterization of a region of the measles virus hemagglutinin sufficient for its dimerization.

Author

Plemper RK, Hammond AL, and Cattaneo R

Subjects
Animals, Biological Transport, Blotting, Western, Chlorocebus aethiops, Cysteine chemistry, Dimerization, Giant Cells virology, Hemagglutinins, Viral genetics, Hemagglutinins, Viral metabolism, Measles virus metabolism, Mutagenesis, Site-Directed, Precipitin Tests, Protein Structure, Tertiary, Vero Cells, Hemagglutinins, Viral chemistry, Measles virus chemistry
Abstract

Attachment of measles virus (MV) to its cellular receptor is mediated by the viral envelope glycoprotein hemagglutinin (H). H exists at the viral surface as a disulfide-linked dimer which may associate into a tetramer. We aimed to define regions of H essential for its homo-oligomerization. To delineate these more precisely, we have generated a series of H ectodomain truncation mutants and studied their abilities to form both homotypic complexes and heterotypic complexes with full-length H. We define a "minimal unit" which is sufficient for MV H dimerization as that encompassing residues 1 to 151. This unit forms both homodimers and heterodimers with full-length H protein, although neither is transported to the cell surface even in the presence of other MV proteins. We show that cysteine residues at positions 139 and 154 are both critical in mediating covalent dimerization, not only of the truncated H mutants but also of full-length MV H protein. Even those cysteine mutants unable to form covalent intermolecular interactions are biologically active, mediating the formation of syncytia, albeit at a reduced rate. We demonstrate that this impaired capacity to mediate cell-to-cell fusion is based mainly on a reduced transport rate of the mutant molecules to the cell surface, indicating a role for covalent intermolecular interactions in efficient transport of MV H dimers to the cell surface.

Published
2000
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18. Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation.

Author

Plemper RK, Bordallo J, Deak PM, Taxis C, Hitt R, and Wolf DH

Subjects
Amino Acid Sequence, Biological Transport, Carboxypeptidases metabolism, Cathepsin A, Cysteine Endopeptidases physiology, Gene Expression Regulation, Fungal, Membrane Glycoproteins genetics, Membrane Transport Proteins, Molecular Sequence Data, Multienzyme Complexes physiology, Mutation, Proteasome Endopeptidase Complex, Protein Binding, Proteins genetics, SEC Translocation Channels, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae metabolism, Ubiquitins physiology, Zinc Fingers physiology, Endoplasmic Reticulum metabolism, Membrane Glycoproteins metabolism, Membrane Proteins metabolism, Proteins metabolism, Saccharomyces cerevisiae Proteins, Ubiquitin-Protein Ligases
Abstract

The endoplasmic reticulum contains a quality control system that subjects misfolded or unassembled secretory proteins to rapid degradation via the cytosolic ubiquitin proteasome system. This requires retrograde protein transport from the endoplasmic reticulum back to the cytosol. The Sec61 pore, the central component of the protein import channel into the endoplasmic reticulum, was identified as the core subunit of the retro-translocon as well. As import of mutated proteins into the endoplasmic reticulum lumen is successfully terminated, a new targeting mechanism must exist that mediates re-entering of misfolded proteins into the Sec61 pore from the lumenal side de novo. The previously identified proteins Der3p/Hrd1p and, as we show here, Hrd3p of the yeast Saccharomyces cerevisiae, are localised in the endoplasmic reticulum membrane and are essential for the degradation of several substrates of the endoplasmic reticulum degradation machinery. Based on genetic studies we demonstrate that they functionally interact with each other and with Sec61p, probably establishing the central part of the retro-translocon. In the absence of Hrd3p, the otherwise stable protein Der3p/Hrd1p becomes rapidly degraded. This depends on a functional ubiquitin proteasome system and the presence of substrate molecules of the endoplasmic reticulum degradation system. When overexpressed, Der3p/Hrd1p accelerates CPY* degradation in Delta(hrd3) cells. Our data suggest a recycling process of Der3p/Hrd1p through Hrd3p. The retro-translocon seems to be build up at least by the Sec61 pore, Der3p/Hrd1p and Hrd3p and mediates both retrograde transport and ubiquitination of substrate molecules.

Published
1999
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19. Retrograde protein translocation: ERADication of secretory proteins in health and disease.

Author

Plemper RK and Wolf DH

Subjects
Biological Transport, Active, Cysteine Endopeptidases metabolism, Cystic Fibrosis etiology, Endoplasmic Reticulum metabolism, Humans, Models, Biological, Multienzyme Complexes metabolism, Neurodegenerative Diseases etiology, Proteasome Endopeptidase Complex, Proteins chemistry, Ubiquitins metabolism, Virus Diseases etiology, Proteins metabolism
Abstract

Eukaryotic cells have a complex degradation machinery that eliminates misfolded or unassembled secretory proteins from the endoplasmic reticulum (ER). The proteins are retained in an ER/pre-Golgi compartment and then hydrolysed by the cytosolic ubiquitin-proteasome system. This requires retrograde translocation of proteins from the ER back to the cytoplasm, which is mediated by Sec61, the central component of the ER protein-import channel. This proteolytic pathway prevents a potentially lethal aggregation of secretory proteins; however, several viruses misuse it to escape detection, and bacterial and plant toxins might also exploit it. Underactive or overactive ER degradation machinery contributes to the pathogenesis of several severe human diseases.

Published
1999
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20. Endoplasmic reticulum degradation. Reverse protein transport and its end in the proteasome.

Author

Plemper RK and Wolf DH

Subjects
Adenosine Triphosphatases metabolism, Biological Transport, Carboxypeptidases metabolism, Cathepsin A, Endoplasmic Reticulum enzymology, Models, Biological, Proteasome Endopeptidase Complex, Saccharomyces cerevisiae enzymology, ATP-Binding Cassette Transporters metabolism, Cysteine Endopeptidases metabolism, Endoplasmic Reticulum metabolism, Membrane Proteins metabolism, Multienzyme Complexes metabolism, Saccharomyces cerevisiae metabolism, Saccharomyces cerevisiae Proteins
Abstract

Degradation of misfolded or unassembled proteins of the secretory pathway is an essential function of the quality control system of the Endoplasmic Reticulum (ER). Using yeast as a model organism we show that a mutated and therefore misfolded soluble lumenal protein carboxypeptidase yscY (CPY), and a polytopic membrane protein, the ATP-binding cassette transporter Pdr5 (Pdr5), are retrograde transported out of the ER and degraded via the cytoplasmic ubiquitin-proteasome system. Retrograde transport depends on an intact Sec61 translocon. Complete import of CPY into the lumen of the ER requests a new targeting mechanism for retrograde transport of the malfolded enzyme through the Sec61 channel to occur. For soluble CPY, but not for the polytopic membrane protein Pdr5 action of the ER-lumenal Hsp70 chaperone Kar2 is necessary to deliver the protein to the ubiquitin-proteasome machinery. Polyubiquitination of CPY and Pdr5 by the ubiquitin conjugating enzymes Ubc6 and Ubc7 is crucial for degradation to occur. Also transport of CPY out of the ER-lumen depends on ubiquitination. Newly discovered proteins of the ER membrane, Derl, Der3/Hrd1, and Hrd3 are specifically involved in the retrograde transport processes.

Published
1999
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21. Re-entering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species.

Author

Plemper RK, Deak PM, Otto RT, and Wolf DH

Subjects
Animals, Biological Transport, Carboxypeptidases genetics, Cathepsin A, Cysteine Endopeptidases physiology, Endoplasmic Reticulum enzymology, Esterases genetics, Esterases metabolism, Glycosylation drug effects, Half-Life, Liver, Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase metabolism, Membrane Proteins genetics, Membrane Transport Proteins, Microsomes metabolism, Models, Biological, Multienzyme Complexes physiology, Proteasome Endopeptidase Complex, Protein Binding, Recombinant Fusion Proteins metabolism, SEC Translocation Channels, Saccharomyces cerevisiae enzymology, Saccharomyces cerevisiae genetics, Saccharomyces cerevisiae Proteins, Swine, Trypsin metabolism, Tunicamycin pharmacology, Carboxypeptidases metabolism, Endoplasmic Reticulum metabolism, Membrane Proteins physiology, Mutation, Saccharomyces cerevisiae metabolism
Abstract

Misfolded or unassembled secretory proteins are retained in the endoplasmic reticulum (ER) and subsequently degraded by the cytosolic ubiquitin-proteasome system. This requires their retrograde transport from the ER lumen into the cytosol, which is mediated by the Sec61 translocon. It had remained a mystery whether ER-localised soluble proteins are at all capable of re-entering the Sec61 channel de novo or whether a permanent contact of the imported protein with the translocon is a prerequisite for retrograde transport. In this study we analysed two new variants of the mutated yeast carboxypeptidase yscY, CPY*: a carboxy-terminal fusion protein of CPY* and pig liver esterase and a CPY* species carrying an additional glycosylation site at its carboxy-terminus. With these constructs it can be demonstrated that the newly synthesised CPY* chain is not retained in the translocation channel but reaches its ER lumenal side completely. Our data indicate that the Sec61 channel provides the essential pore for protein transport through the ER membrane in either direction; persistent contact with the translocon after import seems not to be required for retrograde transport.

Published
1999
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22. The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation.

Author

Dürr G, Strayle J, Plemper R, Elbs S, Klee SK, Catty P, Wolf DH, and Rudolph HK

Subjects
Calcium-Transporting ATPases genetics, Cations, Divalent, Culture Media, Egtazic Acid, Endoplasmic Reticulum metabolism, Fungal Proteins genetics, Fungal Proteins metabolism, Glycosylation, Phenotype, Plasma Membrane Calcium-Transporting ATPases, Receptors, Cell Surface metabolism, Saccharomyces cerevisiae drug effects, Saccharomyces cerevisiae growth & development, Vacuoles, Calcium metabolism, Calcium-Transporting ATPases metabolism, Golgi Apparatus enzymology, Manganese metabolism, Saccharomyces cerevisiae enzymology, Saccharomyces cerevisiae Proteins, Vesicular Transport Proteins
Abstract

The yeast Ca2+ adenosine triphosphatase Pmr1, located in medial-Golgi, has been implicated in intracellular transport of Ca2+ and Mn2+ ions. We show here that addition of Mn2+ greatly alleviates defects of pmr1 mutants in N-linked and O-linked protein glycosylation. In contrast, accurate sorting of carboxypeptidase Y (CpY) to the vacuole requires a sufficient supply of intralumenal Ca2+. Most remarkably, pmr1 mutants are also unable to degrade CpY*, a misfolded soluble endoplasmic reticulum protein, and display phenotypes similar to mutants defective in the stress response to malfolded endoplasmic reticulum proteins. Growth inhibition of pmr1 mutants on Ca2+-deficient media is overcome by expression of other Ca2+ pumps, including a SERCA-type Ca2+ adenosine triphosphatase from rabbit, or by Vps10, a sorting receptor guiding non-native luminal proteins to the vacuole. Our analysis corroborates the dual function of Pmr1 in Ca2+ and Mn2+ transport and establishes a novel role of this secretory pathway pump in endoplasmic reticulum-associated processes.

Published
1998
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23. Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins.

Author

Bordallo J, Plemper RK, Finger A, and Wolf DH

Subjects
Amino Acid Sequence, Base Sequence, Carboxypeptidases genetics, Carboxypeptidases metabolism, Cathepsin A, Cell Division genetics, Cloning, Molecular, Fungal Proteins genetics, Fungal Proteins physiology, Gene Deletion, Intracellular Membranes metabolism, Ligases genetics, Membrane Proteins genetics, Membrane Transport Proteins, Molecular Sequence Data, Mutation, Proteins isolation & purification, SEC Translocation Channels, Saccharomyces cerevisiae, Endoplasmic Reticulum metabolism, Membrane Proteins metabolism, Protein Folding, Proteins genetics, Proteins physiology, Saccharomyces cerevisiae Proteins, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
Abstract

We have studied components of the endoplasmic reticulum (ER) proofreading and degradation system in the yeast Saccharomyces cerevisiae. Using a der3-1 mutant defective in the degradation of a mutated lumenal protein, carboxypeptidase yscY (CPY*), a gene was cloned which encodes a 64-kDa protein of the ER membrane. Der3p was found to be identical with Hrd1p, a protein identified to be necessary for degradation of HMG-CoA reductase. Der3p contains five putative transmembrane domains and a long hydrophilic C-terminal tail containing a RING-H2 finger domain which is oriented to the ER lumen. Deletion of DER3 leads to an accumulation of CPY* inside the ER due to a complete block of its degradation. In addition, a DER3 null mutant allele suppresses the temperature-dependent growth phenotype of a mutant carrying the sec61-2 allele. This is accompanied by the stabilization of the Sec61-2 mutant protein. In contrast, overproduction of Der3p is lethal in a sec61-2 strain at the permissive temperature of 25 degrees C. A mutant Der3p lacking 114 amino acids of the lumenal tail including the RING-H2 finger domain is unable to mediate degradation of CPY* and Sec61-2p. We propose that Der3p acts prior to retrograde transport of ER membrane and lumenal proteins to the cytoplasm where they are subject to degradation via the ubiquitin-proteasome system. Interestingly, in ubc6-ubc7 double mutants, CPY* accumulates in the ER, indicating the necessity of an intact cytoplasmic proteolysis machinery for retrograde transport of CPY*. Der3p might serve as a component programming the translocon for retrograde transport of ER proteins, or it might be involved in recognition through its lumenal RING-H2 motif of proteins of the ER that are destined for degradation.

Published
1998
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24. Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation.

Author

Plemper RK, Böhmler S, Bordallo J, Sommer T, and Wolf DH

Subjects
Biological Transport, Carboxypeptidases metabolism, Fungal Proteins genetics, HSP70 Heat-Shock Proteins genetics, Ligases metabolism, Membrane Proteins genetics, Mutation, SEC Translocation Channels, Endoplasmic Reticulum metabolism, Fungal Proteins metabolism, HSP70 Heat-Shock Proteins metabolism, Heat-Shock Proteins, Membrane Proteins metabolism, Membrane Transport Proteins, Saccharomyces cerevisiae Proteins, Ubiquitin-Conjugating Enzymes
Abstract

Proteins enter the secretory pathway through the endoplasmic reticulum, which delivers properly folded proteins to their site of action and contains a quality-control system to monitor and prevent abnormal proteins from being delivered. Many of these proteins are degraded by the cytoplasmic proteasome, which requires their retrograde transport to the cytoplasm. Based on a co-immunoprecipitation of major histocompatibility complex (MHC) class I heavy-chain breakdown intermediates with the translocon subunit Sec61p, it was speculated that Sec61p maybe involved in retrograde transport. Here we present functional evidence from genetic studies that Sec61p mediates retrograde transport of a mutated lumenal yeast carboxypeptidase ycsY (CPY*) in vivo. The endoplasmic reticulum lumenal chaperone BiP (Kar2p) and Sec63p, which are also subunits of the import machinery, are involved in export of CPY* to the cytosol. Thus our results demonstrate that retrograde transport of proteins is mediated by a functional translocon. We consider the export of endoplasmic reticulum-localized proteins to the cytosol by the translocon for proteasome degradation to be a general process in eukaryotic cell biology.

Published
1997
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